1hi0: Difference between revisions
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[[Image:1hi0.gif|left|200px]]<br /><applet load="1hi0" size=" | [[Image:1hi0.gif|left|200px]]<br /><applet load="1hi0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hi0, resolution 3.0Å" /> | caption="1hi0, resolution 3.0Å" /> | ||
'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX'''<br /> | '''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HI0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6] with MN, MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=CA1:The Three Conserved Active Site Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The Three Conserved Active Site Aspartate'>CA2</scene>, <scene name='pdbsite=CA3:The Three Conserved Active Site Aspartate'>CA3</scene>, <scene name='pdbsite=GP1:Gtp Binding Site For Residue P666'>GP1</scene>, <scene name='pdbsite=GP2:Gtp Binding Site For Residue P667'>GP2</scene>, <scene name='pdbsite=GQ1:Gtp Binding Site For Residue Q666'>GQ1</scene>, <scene name='pdbsite=GQ2:Gtp Binding Site For Residue Q667'>GQ2</scene>, <scene name='pdbsite=GR1:Gtp Binding Site For Residue R666'>GR1</scene> and <scene name='pdbsite=GR2:Gtp Binding Site For Residue R667'>GR2</scene>. Full crystallographic information is available from [http:// | 1HI0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=CA1:The+Three+Conserved+Active+Site+Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The+Three+Conserved+Active+Site+Aspartate'>CA2</scene>, <scene name='pdbsite=CA3:The+Three+Conserved+Active+Site+Aspartate'>CA3</scene>, <scene name='pdbsite=GP1:Gtp+Binding+Site+For+Residue+P666'>GP1</scene>, <scene name='pdbsite=GP2:Gtp+Binding+Site+For+Residue+P667'>GP2</scene>, <scene name='pdbsite=GQ1:Gtp+Binding+Site+For+Residue+Q666'>GQ1</scene>, <scene name='pdbsite=GQ2:Gtp+Binding+Site+For+Residue+Q667'>GQ2</scene>, <scene name='pdbsite=GR1:Gtp+Binding+Site+For+Residue+R666'>GR1</scene> and <scene name='pdbsite=GR2:Gtp+Binding+Site+For+Residue+R667'>GR2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: viral polymerase]] | [[Category: viral polymerase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:49:18 2008'' | ||
Revision as of 10:49, 3 February 2008
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RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX
OverviewOverview
In most RNA viruses, genome replication and transcription are catalysed by, a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform, these operations in a capsid (the polymerase complex), using an enzyme, that can read both single- and double-stranded RNA. Structures have been, solved for such viral capsids, but they do not resolve the polymerase, subunits in any detail. Here we show that the 2 A resolution X-ray, structure of the active polymerase subunit from the double-stranded RNA, bacteriophage straight phi6 is highly similar to that of the polymerase of, hepatitis C virus, providing an evolutionary link between double-stranded, RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with, oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a, mechanism by which the incoming double-stranded RNA is opened up to feed, the template through to the active site, while the substrates enter by, another route. The template strand initially overshoots, locking into a, specificity pocket, and then, in the presence of cognate NTPs, reverses to, form the initiation complex; this process engages two NTPs, one of which, acts with the carboxy-terminal domain of the protein to prime the, reaction. Our results provide a working model for the initiation of, replication and transcription.
About this StructureAbout this Structure
1HI0 is a Single protein structure of sequence from Bacteriophage phi-6 with , and as ligands. Known structural/functional Sites: , , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
A mechanism for initiating RNA-dependent RNA polymerization., Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI, Nature. 2001 Mar 8;410(6825):235-40. PMID:11242087
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